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Database: UniProt
Entry: A0A1A6HND4_NEOLE
LinkDB: A0A1A6HND4_NEOLE
Original site: A0A1A6HND4_NEOLE 
ID   A0A1A6HND4_NEOLE        Unreviewed;       349 AA.
AC   A0A1A6HND4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE   Flags: Fragment;
GN   ORFNames=A6R68_22039 {ECO:0000313|EMBL:OBS79759.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS79759.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS79759.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS79759.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS79759.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC         glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00000251,
CC         ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|RuleBase:RU610713}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS79759.1}.
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DR   EMBL; LZPO01018093; OBS79759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A6HND4; -.
DR   STRING; 56216.A0A1A6HND4; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF17; HYALURONIDASE PH-20; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   PRINTS; PR00848; SPERMPH20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092124}.
FT   ACT_SITE        148
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   DISULFID        224..238
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   NON_TER         349
FT                   /evidence="ECO:0000313|EMBL:OBS79759.1"
SQ   SEQUENCE   349 AA;  40338 MW;  210D20ACE70CEC41 CRC64;
     MGGLRVKHLY WGSFVESGGT FQSVLIIFLL IPCSLTVDYR AIPLLPNETF LWIWNVPTEA
     CIGQFNHSID LSLFPLIGSP RKTATGQPVT LFYVDRLGYY PHIDTRMREH HGGIPQLGNL
     QNHLTKARTD IEHYIPVDRL GLAVIDWEEW RPTWLRNWRP KDIYRNKSID LVQANNAGIS
     ISDATRQAKS AFEAAGRQFM EETLRLGKSV RPKYLWGYYL FPDCYNNKFQ DPNYDGKCPN
     VEKQRNDDLS WMWRESTGLY PSVYLKRDLK SNRQATLYVR FRVVESIRVS KVRNESDPVP
     IFVYTRLVFT DNITEYLLEE DLVNTIGEIV ALGPAGIIIW DAMTLAQRA
//
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